EC Number |
General Stability |
Reference |
---|
3.1.3.2 | 5 M urea, 2 h, 71% of the initial activity is retained |
134736 |
3.1.3.2 | 50% loss of activity after lyophilization |
134801 |
3.1.3.2 | 50-60% loss of activity after two freeze-thaw cycles |
134704 |
3.1.3.2 | deglycosylated enzyme is more susceptible than native enzyme to denaturation with guanidine hydrochloride |
134718 |
3.1.3.2 | denaturation by guanidine hydrochloride and SDS |
134736 |
3.1.3.2 | enzyme maintains its catalytic activity after succinylation of 52 free amino groups per molecule. Free amino groups may play an important role in the maintenance of enzyme stability at pH values greater than pH 5.4 |
134775 |
3.1.3.2 | enzyme shows strong resistance toward pepsin and trypsin |
707770 |
3.1.3.2 | freezing denatures the enzyme |
134707 |
3.1.3.2 | loses more than 90% of activity in 3 M urea at 25°C, pH 7.0 |
134750 |
3.1.3.2 | pepsin treatment, 15 min, native enzyme loses 20% of the original activity, the deglycosylated enzyme is completely inactivated |
134718 |